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Preparation of Peptide Selenoesters from Their Corresponding Acyl Hydrazides †
Author(s) -
Li Yunxue,
Liu Jiazhi,
Zhou Qingqing,
Zhao Jie,
Wang Ping
Publication year - 2021
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.202100086
Subject(s) - chemistry , thioester , native chemical ligation , peptide , hydrazide , chemical ligation , combinatorial chemistry , racemization , yield (engineering) , ligation , peptide synthesis , reactivity (psychology) , thio , protecting group , cysteine , stereochemistry , organic chemistry , biochemistry , alkyl , enzyme , microbiology and biotechnology , medicine , materials science , alternative medicine , pathology , metallurgy , biology
Main observation and conclusion Selenoesters are useful substitutes for traditional thioesters in protein ligation chemistry due to their high reactivity in the trans ‐thio/selenoesterification reaction. However, existing synthetic routes to access peptide selenoester require a selenoesterification reaction between a selenide and a protected peptide with a free carboxylate at the C‐terminus. Herein, we introduce an efficient method to convert peptide acyl hydrazide, a convenient thioester surrogate, into the desired selenoester for peptide ligation. Our methodology can be applied to fully de‐protected peptides with various C‐terminal amino acid residues in high yield without racemization. We believe that this method provides a useful alternative to access peptide C‐terminal selenoesters for protein ligation.